芍药苷、马钱苷与牛血清白蛋白相互作用的研究  

Investigation of the interaction between bovine serum albumin with paeoniflorin and loganin

作　　者：温海燕[1] 章弘扬[1] 王月荣[1] 张秀瑾[2] 胡坪[1] 

机构地区：[1]华东理工大学化学与分子工程学院,上海200237 [2]华东理工大学化工学院,上海200237

出　　处：《药物分析杂志》2010年第1期6-11,共6页Chinese Journal of Pharmaceutical Analysis

基　　金：国家科技支撑项目(2006BAI08B03-07)资助

摘　　要：目的:研究中药活性小分子芍药苷、马钱苷与牛血清白蛋白(BSA)之间的相互作用机制。方法:采用荧光光谱法、同步荧光光谱法和紫外光谱法测定芍药苷和马钱苷与BSA的结合常数与结合位点数,根据热力学方程计算作用力类型。结果:2种苷类化合物与BSA的静态结合常数分别为3.56×104和9.06×104L.mol-1,作用位点数n分别为0.624和0.853,猝灭作用主要属于静态猝灭。热力学参数表明该结合过程是一个熵增的自发过程。结论:芍药苷与马钱苷和BSA的结合作用力均为疏水力,两化合物可以嵌插到BSA疏水腔内,与BSA形成复合物。Objective：To study the interaction of paeoniflorin and loganin with bovine serum albumin（BSA） in buffer solutions.Methods：Fluorescence spectroscopy,UV-vis spectroscopy and synchronous fluorescence spectroscopy were used to characterize the interaction between BSA with paeoniflorin and loganin.The binding constants（KLB） and the number of binding sites（n） were obtained at different temperatures respectively,the binding forces were calculated via thermodynamic equation.Results：KLB of paeoniflorin-BSA and loganin-BSA were 3.56×104（n=0.624） and 9.06×104 L·mol-1（n=0.853）,respectively.The fluoresence quenching of BSA caused by paeoniflorin or loganin was a static quenching process.Thermodynamic parameters showed that binding process of paeoniflorin and loganin with BSA was a spontaneous interaction procedure in which entropy increased while Gibbs free energy decreased.Conclusion：Paeoniflorin and loganin can be intercalated into the hydrophobic pockets of BSA by hydrophobic force.

关 键 词：芍药苷 马钱苷 牛血清白蛋白 荧光光谱 紫外光谱 相互作用 

分 类 号：R917[医药卫生—药物分析学]